RPN3_ENCCU
ID RPN3_ENCCU Reviewed; 376 AA.
AC Q8SRT7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=26S proteasome regulatory subunit RPN3;
GN Name=RPN3; OrderedLocusNames=ECU05_1540;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which
CC degrades poly-ubiquitinated proteins in the cytoplasm and in the
CC nucleus. It is essential for the regulated turnover of proteins and for
CC the removal of misfolded proteins. The proteasome is a multicatalytic
CC proteinase complex that is characterized by its ability to cleave
CC peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group
CC at neutral or slightly basic pH (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family. {ECO:0000305}.
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DR EMBL; AL590445; CAD26674.1; -; Genomic_DNA.
DR RefSeq; NP_597497.1; NM_001041363.1.
DR AlphaFoldDB; Q8SRT7; -.
DR SMR; Q8SRT7; -.
DR STRING; 284813.Q8SRT7; -.
DR GeneID; 859164; -.
DR KEGG; ecu:ECU05_1540; -.
DR VEuPathDB; MicrosporidiaDB:ECU05_1540; -.
DR HOGENOM; CLU_062465_0_0_1; -.
DR InParanoid; Q8SRT7; -.
DR OMA; SCIENDI; -.
DR OrthoDB; 883706at2759; -.
DR Proteomes; UP000000819; Chromosome V.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01399; PCI; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT CHAIN 1..376
FT /note="26S proteasome regulatory subunit RPN3"
FT /id="PRO_0000382764"
FT DOMAIN 159..336
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 376 AA; 43371 MW; B514471A6069BCC1 CRC64;
MDEKECVAEL VDVLSQLSSN REEAMDRYER QVFTFIRNIK PETLDSLNLE SELERIAAYP
VILGALFMRK EFKKIDKIVN ENLLSHLIGK KRVYDYFVGL IVKFLYLARK NECQDNSALF
SLLVTNKELG NEYTVSVITN CLLDMLIGNK IFQRIDNSIV TTSEQARYNY YNGIIFMVEG
DYESALKCFH TCVILSTNRD LVLGAEKRVI LCMLLSSDYS IPYPCKPSLR IYFKLASAVK
RADIKKFEET LESNKDELMS QGLYFVAKRL SQNVIQEGIR KISVVYSRIS YEDIAHILGI
NSGEVEYLVK RTIRKGLIKG KVADGIFYSL REDKSKTDIG IGIRDCIQLA NYIQEHMRYP
AIEPLCYEKV RKVHDK